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ATPase activities in partially purified membranes of Acetabularia

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Abstract

Partly purified membranes (with plasmalemma material) of Acetabularia mediterranea were studied with respect to ATPase activity in alkali- and Ca++-free media and its sensitivity to pH (5 – 9), oligomycin (200 ώg/mg protein), 100 ώM N-N′-dicyclohexylcarbodiimide (DCCD), and 50 ώM vanadate. Besides activities which may originate from mitochondrial H+ ATPase (oligomycin-sensitive, alkaline pH optimum) and tonoplast H+ ATPase (DCCD-sensitive, pH optimum 7.5), there is ATPase activity with a pH optimum around pH 6.5, sensitive to vanadate and insensitive to DCCD. These results strongly suggest that the electrogenic Cl pump in the plasmalemma of Acetabularia is an ATPase. Effects of Mg++, Mg-ATP, ADP, GTP, UTP, CTP and HCO3 versus Cl on this ATPase activity are described.

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Communicated by P. Matile

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Goldfarb, V., Gradmann, D. ATPase activities in partially purified membranes of Acetabularia . Plant Cell Reports 2, 152–155 (1983). https://doi.org/10.1007/BF00269342

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  • DOI: https://doi.org/10.1007/BF00269342

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